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Conserved domains on  [gi|446463179|ref|WP_000541033|]
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MULTISPECIES: tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG [Bacillus]

Protein Classification

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA( domain architecture ID 11418560)

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA such as tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG, which is involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34

CATH:  1.10.10.1800
EC:  2.1.1.-
Gene Ontology:  GO:0050660|GO:0002098|GO:0030488|GO:0008033
PubMed:  18565343|19801413|19767610|11544186
SCOP:  4006485

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 3-627 0e+00

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 1256.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   3 YNAGSYDVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQM 82
Cdd:COG0445    2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  83 RMLNTGKGPAVRALRAQADKFSYQHELKKTIEETPNLTLFQGMVERLIVEDGECKGVITQAGAEYTAKTVVITTGTFLRG 162
Cdd:COG0445   82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 163 EIIMGDLKYSSGPNNQQPSITLSEHLEELGFDLVRFKTGTPPRVNSNTIDYSKTEIQPGDDKPRAFSFETTKFIMDQIPC 242
Cdd:COG0445  162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 243 WLTYTSTETHRLIDENLHRSAMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQR 322
Cdd:COG0445  242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 323 DMLRTIPGLENVEMMRTGYAIEYDAIVPTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINAACRSLGKKEVI 402
Cdd:COG0445  322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 403 LGREDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHEIGLIKEERYERFTNKKLQIEQEKERLSS 482
Cdd:COG0445  402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 483 IIIKPRPEVQELIRNIGGSELKDGIRASDLLRRPEMTYEHIHLLVPSEVELSDEVTEQVEIQIKYEGYIEKSLQQVERMK 562
Cdd:COG0445  482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446463179 563 KMESKKIPVDIDYDAISSLASEARQKLKDVRPLSVGQASRISGVNPADISILLVYIEQGKIARVS 627
Cdd:COG0445  562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 3-627 0e+00

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 1256.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   3 YNAGSYDVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQM 82
Cdd:COG0445    2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  83 RMLNTGKGPAVRALRAQADKFSYQHELKKTIEETPNLTLFQGMVERLIVEDGECKGVITQAGAEYTAKTVVITTGTFLRG 162
Cdd:COG0445   82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 163 EIIMGDLKYSSGPNNQQPSITLSEHLEELGFDLVRFKTGTPPRVNSNTIDYSKTEIQPGDDKPRAFSFETTKFIMDQIPC 242
Cdd:COG0445  162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 243 WLTYTSTETHRLIDENLHRSAMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQR 322
Cdd:COG0445  242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 323 DMLRTIPGLENVEMMRTGYAIEYDAIVPTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINAACRSLGKKEVI 402
Cdd:COG0445  322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 403 LGREDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHEIGLIKEERYERFTNKKLQIEQEKERLSS 482
Cdd:COG0445  402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 483 IIIKPRPEVQELIRNIGGSELKDGIRASDLLRRPEMTYEHIHLLVPSEVELSDEVTEQVEIQIKYEGYIEKSLQQVERMK 562
Cdd:COG0445  482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446463179 563 KMESKKIPVDIDYDAISSLASEARQKLKDVRPLSVGQASRISGVNPADISILLVYIEQGKIARVS 627
Cdd:COG0445  562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 8-622 0e+00

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 1071.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    8 YDVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   88 GKGPAVRALRAQADKFSYQHELKKTIEETPNLTLFQGMVERLIVED-GECKGVITQAGAEYTAKTVVITTGTFLRGEIIM 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  167 GDLKYSSGPNNQQPSITLSEHLEELGFDLVRFKTGTPPRVNSNTIDYSKTEIQPGDDKPRAFSFETTKFIMDQIPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  247 TSTETHRLIDENLHRSAMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQRDMLR 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  327 TIPGLENVEMMRTGYAIEYDAIVPTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINAACRSLGKKEVILGRE 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHEIGLIKEERYERFTNKKLQIEQEKERLSSIIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  487 PRPEVQELIRNIGGSELKDGIRASDLLRRPEMTYEHIHLLVPSEVELSDEVTEQVEIQIKYEGYIEKSLQQVERMKKMES 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446463179  567 KKIPVDIDYDAISSLASEARQKLKDVRPLSVGQASRISGVNPADISILLVYIEQGK 622
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
9-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 696.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    9 DVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNTG 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   89 KGPAVRALRAQADKFSYQHELKKTIEETPNLTLFQGMVERLIVEDGECKGVITQAGAEYTAKTVVITTGTFLRGEIIMGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  169 LKYSSGPNNQQPSITLSEHLEELGFDLVRFKTGTPPRVNSNTIDYSKTEIQPGDDKPRAFSFETTKFIMDQIPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  249 TETHRLIDENLHRSAMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQRDMLRTI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446463179  329 PGLENVEMMRTGYAIEYDAIVPTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINAACRSLGKK 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 311-414 6.23e-19

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 89.82  E-value: 6.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 311 GLSTSL--PEdvQRDMLRTIPGLENVEMMRTGyaieydaiV---------PTQLWPTLETKKIKNLYTAGQINGTSGYEE 379
Cdd:PRK05335 278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446463179 380 AAGQGLMAGINAACRSLGKKEVILGREDAyIGVLI 414
Cdd:PRK05335 348 SAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 3-627 0e+00

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 1256.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   3 YNAGSYDVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQM 82
Cdd:COG0445    2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  83 RMLNTGKGPAVRALRAQADKFSYQHELKKTIEETPNLTLFQGMVERLIVEDGECKGVITQAGAEYTAKTVVITTGTFLRG 162
Cdd:COG0445   82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 163 EIIMGDLKYSSGPNNQQPSITLSEHLEELGFDLVRFKTGTPPRVNSNTIDYSKTEIQPGDDKPRAFSFETTKFIMDQIPC 242
Cdd:COG0445  162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 243 WLTYTSTETHRLIDENLHRSAMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQR 322
Cdd:COG0445  242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 323 DMLRTIPGLENVEMMRTGYAIEYDAIVPTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINAACRSLGKKEVI 402
Cdd:COG0445  322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 403 LGREDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHEIGLIKEERYERFTNKKLQIEQEKERLSS 482
Cdd:COG0445  402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 483 IIIKPRPEVQELIRNIGGSELKDGIRASDLLRRPEMTYEHIHLLVPSEVELSDEVTEQVEIQIKYEGYIEKSLQQVERMK 562
Cdd:COG0445  482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446463179 563 KMESKKIPVDIDYDAISSLASEARQKLKDVRPLSVGQASRISGVNPADISILLVYIEQGKIARVS 627
Cdd:COG0445  562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 8-622 0e+00

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 1071.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    8 YDVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNT 87
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   88 GKGPAVRALRAQADKFSYQHELKKTIEETPNLTLFQGMVERLIVED-GECKGVITQAGAEYTAKTVVITTGTFLRGEIIM 166
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  167 GDLKYSSGPNNQQPSITLSEHLEELGFDLVRFKTGTPPRVNSNTIDYSKTEIQPGDDKPRAFSFETTKFIMDQIPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  247 TSTETHRLIDENLHRSAMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQRDMLR 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  327 TIPGLENVEMMRTGYAIEYDAIVPTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINAACRSLGKKEVILGRE 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHEIGLIKEERYERFTNKKLQIEQEKERLSSIIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  487 PRPEVQELIRNIGGSELKDGIRASDLLRRPEMTYEHIHLLVPSEVELSDEVTEQVEIQIKYEGYIEKSLQQVERMKKMES 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446463179  567 KKIPVDIDYDAISSLASEARQKLKDVRPLSVGQASRISGVNPADISILLVYIEQGK 622
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
9-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 696.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    9 DVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMGRNIDKTHIQMRMLNTG 88
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   89 KGPAVRALRAQADKFSYQHELKKTIEETPNLTLFQGMVERLIVEDGECKGVITQAGAEYTAKTVVITTGTFLRGEIIMGD 168
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  169 LKYSSGPNNQQPSITLSEHLEELGFDLVRFKTGTPPRVNSNTIDYSKTEIQPGDDKPRAFSFETTKFIMDQIPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  249 TETHRLIDENLHRSAMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQRDMLRTI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446463179  329 PGLENVEMMRTGYAIEYDAIVPTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINAACRSLGKK 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 401-615 1.39e-129

tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA and to be responsible for the interaction with protein MnmE. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, pfam12631.


Pssm-ID: 464049 [Multi-domain]  Cd Length: 214  Bit Score: 379.42  E-value: 1.39e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  401 VILGREDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTEIGHEIGLIKEERYERFTNKKLQIEQEKERL 480
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  481 SSIIIKPRPEVQELIrNIGGSELKDGIRASDLLRRPEMTYEHIHLLVPSEVELSDEVTEQVEIQIKYEGYIEKSLQQVER 560
Cdd:pfam13932  81 KSTRLSPSEWNNALL-ELGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446463179  561 MKKMESKKIPVDIDYDAISSLASEARQKLKDVRPLSVGQASRISGVNPADISILL 615
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 311-414 6.23e-19

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 89.82  E-value: 6.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 311 GLSTSL--PEdvQRDMLRTIPGLENVEMMRTGyaieydaiV---------PTQLWPTLETKKIKNLYTAGQINGTSGYEE 379
Cdd:PRK05335 278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446463179 380 AAGQGLMAGINAACRSLGKKEVILGREDAyIGVLI 414
Cdd:PRK05335 348 SAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 321-414 2.00e-18

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 88.19  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179 321 QRDMLRTIPGLENVEMMRTGyaieydaiV---------PTQLWPTLETKKIKNLYTAGQINGTSGYEEAAGQGLMAGINA 391
Cdd:COG1206  288 QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINA 359

                         90       100
                 ....*....|....*....|...
gi 446463179 392 ACRSLGKKEVILGREDAyIGVLI 414
Cdd:COG1206  360 ARLLLGKEPVPPPPTTA-LGALL 381
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
8-157 3.08e-10

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 61.67  E-value: 3.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   8 YDVIVIGAGHAGCEAGLAAARMGSKTLMLtinldmvafmpcnpsvggpakgivvrEIDALGGEMGR-----NI--DKTHI 80
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATtkeieNYpgFPEGI 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446463179  81 QmrmlntgkGPA-VRALRAQADKFsyqhelkktieetpNLTLFQGMVERlIVEDGECKGVITQAGAEYTAKTVVITTG 157
Cdd:COG0492   55 S--------GPElAERLREQAERF--------------GAEILLEEVTS-VDKDDGPFRVTTDDGTEYEAKAVIIATG 109
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 8-157 1.72e-06

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 50.60  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   8 YDVIVIGAGHAGCEAGLAAARMGSKTLMLT---------------INL-------------------DMVAFM--PCNPS 51
Cdd:COG1053    4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaagedspeehfyDTVKGGdgLADQD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  52 V------GGPAkgiVVREIDALGGEMGRNIDKTHIQM------RMLNTGK--GPA-VRALRAQADKfsyqHELKKtIEET 116
Cdd:COG1053   84 LvealaeEAPE---AIDWLEAQGVPFSRTPDGRLPQFgghsvgRTCYAGDgtGHAlLATLYQAALR----LGVEI-FTET 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446463179 117 PnltlfqgmVERLIVEDGECKGVI--TQAGAEYT--AKTVVITTG 157
Cdd:COG1053  156 E--------VLDLIVDDGRVVGVVarDRTGEIVRirAKAVVLATG 192
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 9-157 6.72e-06

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 48.76  E-value: 6.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    9 DVIVIGAGHAGCEAGLAAARMGSKTLMLtinldmvafMPcNPSVGGpakgivvreidALGGEMGRNIDKTHIQMRMLNTG 88
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLV---------ER-RGFLGG-----------MLTSGLVGPDMGFYLNKEQVVGG 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   89 -----------KGPAVRALRAQADKFSYQHE-LKKTIEE---TPNLT-LFQGMVERLIVEDGECKGVIT---QAGAEYTA 149
Cdd:pfam12831  60 iarefrqrlraRGGLPGPYGLRGGWVPFDPEvAKAVLDEmlaEAGVTvLLHTRVVGVVKEGGRITGVTVetkGGRITIRA 139


                  ....*...
gi 446463179  150 KTVVITTG 157
Cdd:pfam12831 140 KVFIDATG 147
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 8-157 1.53e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 44.23  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    8 YDVIVIGAGHAGCEAGLAAARMGSKTLMLTINlDMVAFMPCnpsvGGPAKGIVVREIDALGGEMGRNIDKTHIQM---RM 84
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARFFSpngDS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446463179   85 LN----TGKGPAVRalRAQADKFSYQHELKKTIEETPNLTlfqgmVERLIVEDGECKGVITQAGAEYTAKTVVITTG 157
Cdd:TIGR02032  76 VEipieTELAYVID--RDAFDEQLAERAQEAGAELRLGTR-----VLDVEIHDDRVVVIVRGSEGTVTAKIVIGADG 145
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
8-37 1.98e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 44.07  E-value: 1.98e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 446463179   8 YDVIVIGAGHAGCEAGLAAARMGSKTLMLT 37
Cdd:PRK05329   3 FDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 8-158 9.11e-04

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 42.00  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   8 YDVIVIGAGHAGCEAGLAAARMGSKTLMltINLDMvafmpcnpsVGG--------PAKGIV----VREIDALGGEMGRNI 75
Cdd:COG1249    4 YDLVVIGAGPGGYVAAIRAAQLGLKVAL--VEKGR---------LGGtclnvgciPSKALLhaaeVAHEARHAAEFGISA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179  76 DKTHIQMrmlntgkgPAVRA-LRAQADKFS--YQHELKKtieetPNLTLFQGMVE-----RLIVEDGEckgvitqagaEY 147
Cdd:COG1249   73 GAPSVDW--------AALMArKDKVVDRLRggVEELLKK-----NGVDVIRGRARfvdphTVEVTGGE----------TL 129

                        170
                 ....*....|.
gi 446463179 148 TAKTVVITTGT 158
Cdd:COG1249  130 TADHIVIATGS 140
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 9-159 2.51e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 40.73  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    9 DVIVIGAGHAGCEAGLAAARMGSKTLMLT---------------INL--------------------------------- 40
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkgqpfggatawssggIDAlgnppqggidspelhptdtlkgldeladhpyve 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179   41 -------DMVA-----FMPCNPSVGGPakgIVVREidaLGGEmgRNIDKTHIQM----RMLNTGKGPAVRaLRAQADKfs 104
Cdd:pfam00890  81 afveaapEAVDwlealGVPFSRTEDGH---LDLRP---LGGL--SATWRTPHDAadrrRGLGTGHALLAR-LLEGLRK-- 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446463179  105 YQHELkktieetpnltLFQGMVERLIVEDGECKGVITQAGAE-----YTAKT-VVITTGTF 159
Cdd:pfam00890 150 AGVDF-----------QPRTAADDLIVEDGRVTGAVVENRRNgrevrIRAIAaVLLATGGF 199
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 8-157 2.73e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 40.38  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446463179    8 YDVIVIGAGHAGCEAGLAAARMGSKTLMLTINLDMVAFmPCNPSvggpakgivvreiDALGGEMGRnidkthiqmrmLNT 87
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPYG-GCVLS-------------KALLGAAEA-----------PEI 55

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446463179   88 GKGPAVRALRAQADKFSYQHELKKTIEETpnltlfqgmVERLIVEDGECKGVITQAG--AEYTAKTVVITTG 157
Cdd:pfam07992  56 ASLWADLYKRKEEVVKKLNNGIEVLLGTE---------VVSIDPGAKKVVLEELVDGdgETITYDRLVIATG 118
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
8-33 3.14e-03

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 40.16  E-value: 3.14e-03
                         10        20
                 ....*....|....*....|....*.
gi 446463179   8 YDVIVIGAGHAGCEAGLAAARMGSKT 33
Cdd:COG3075    3 FDVVVIGGGLAGLTAAIRAAEAGLRV 28
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
7-36 4.45e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 39.86  E-value: 4.45e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 446463179   7 SYDVIVIGAGHAGCEAGLAAARMGSKTLML 36
Cdd:PRK08274   4 MVDVLVIGGGNAALCAALAAREAGASVLLL 33
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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